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Protein

mRNA-capping enzyme subunit alpha

Gene

CEG1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Second step of mRNA capping. Transfer of the GMP moiety of GTP to the 5'-end of RNA via an enzyme-GMP covalent reaction intermediate.

Catalytic activityi

GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.

Cofactori

a divalent metal cationNote: Divalent metal ions.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei70 – 701N6-GMP-lysine intermediate1 Publication

GO - Molecular functioni

  • GTP binding Source: UniProtKB-KW
  • mRNA guanylyltransferase activity Source: SGD

GO - Biological processi

  • 7-methylguanosine mRNA capping Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

mRNA capping, mRNA processing

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:G3O-30626-MONOMER.
YEAST:G3O-30626-MONOMER.
ReactomeiR-SCE-72086. mRNA Capping.
R-SCE-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA-capping enzyme subunit alpha
Alternative name(s):
GTP--RNA guanylyltransferase
Short name:
GTase
mRNA guanylyltransferase (EC:2.7.7.50)
Gene namesi
Name:CEG1
Ordered Locus Names:YGL130W
ORF Names:G2853
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL130W.
SGDiS000003098. CEG1.

Subcellular locationi

GO - Cellular componenti

  • mRNA cap methyltransferase complex Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi57 – 571E → A: No effect. 1 Publication
Mutagenesisi58 – 581E → A: No effect. 1 Publication
Mutagenesisi59 – 591K → A, T, S or R: No effect. 1 Publication
Mutagenesisi66 – 661Y → A: Temperature-sensitive. 1 Publication
Mutagenesisi70 – 701K → A, R, M, I or T: Lethal. 1 Publication
Mutagenesisi71 – 711T → A: No effect. 1 Publication
Mutagenesisi72 – 721D → A: No effect. 1 Publication
Mutagenesisi73 – 731G → A: Lethal. 1 Publication
Mutagenesisi95 – 951D → A: Temperature-sensitive. 1 Publication
Mutagenesisi96 – 961R → A: Temperature-sensitive. 1 Publication
Mutagenesisi97 – 971E → A: Temperature-sensitive. 1 Publication
Mutagenesisi107 – 1093RFP → AAA: Reduced growth at 25 degrees and lethal at 37 degrees. 1 Publication
Mutagenesisi114 – 1141K → A: No effect. 1 Publication
Mutagenesisi115 – 1151K → A: No effect. 1 Publication
Mutagenesisi116 – 1161K → A: No effect. 1 Publication
Mutagenesisi117 – 1171E → A: No effect. 1 Publication
Mutagenesisi118 – 1181E → A: No effect. 1 Publication
Mutagenesisi129 – 1291L → A: No effect. 1 Publication
Mutagenesisi130 – 1301D → A: Lethal. 1 Publication
Mutagenesisi131 – 1311G → A: Temperature-sensitive. 1 Publication
Mutagenesisi132 – 1321E → A: Lethal. 1 Publication
Mutagenesisi134 – 1341V → A: No effect. 1 Publication
Mutagenesisi218 – 2181D → A: No effect. 1 Publication
Mutagenesisi219 – 2191K → A: No effect. 1 Publication
Mutagenesisi225 – 2251D → A: Lethal. 1 Publication
Mutagenesisi226 – 2261G → A: Lethal. 1 Publication
Mutagenesisi241 – 2411K → A: No effect. 1 Publication
Mutagenesisi242 – 2421D → A: No effect. 1 Publication
Mutagenesisi249 – 2491K → A: Lethal. 1 Publication
Mutagenesisi253 – 2531E → A: No effect. 1 Publication
Mutagenesisi254 – 2541N → A: No effect. 1 Publication
Mutagenesisi255 – 2551T → A: Temperature-sensitive. 1 Publication
Mutagenesisi257 – 2571D → A: Lethal. 1 Publication
Mutagenesisi274 – 2741K → A: No effect. 1 Publication
Mutagenesisi275 – 2751D → A: No effect. 1 Publication
Mutagenesisi276 – 2761D → A: No effect. 1 Publication
Mutagenesisi395 – 3951E → A: No effect. 1 Publication
Mutagenesisi396 – 3961D → A: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 459459mRNA-capping enzyme subunit alphaPRO_0000210106Add
BLAST

Proteomic databases

MaxQBiQ01159.
PeptideAtlasiQ01159.

PTM databases

iPTMnetiQ01159.

Interactioni

Subunit structurei

The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an RNA 5'-triphosphatase.

Binary interactionsi

WithEntry#Exp.IntActNotes
CET1O132977EBI-10503,EBI-4473

Protein-protein interaction databases

BioGridi33121. 86 interactions.
DIPiDIP-2298N.
IntActiQ01159. 26 interactions.
MINTiMINT-621589.

Structurei

Secondary structure

1
459
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 3313Combined sources
Helixi38 – 403Combined sources
Beta strandi47 – 504Combined sources
Helixi53 – 586Combined sources
Beta strandi61 – 633Combined sources
Beta strandi65 – 717Combined sources
Beta strandi73 – 8210Combined sources
Turni84 – 863Combined sources
Beta strandi89 – 946Combined sources
Beta strandi96 – 983Combined sources
Beta strandi100 – 1034Combined sources
Helixi118 – 1203Combined sources
Beta strandi126 – 13712Combined sources
Turni139 – 1413Combined sources
Beta strandi144 – 15613Combined sources
Beta strandi162 – 1654Combined sources
Helixi166 – 17510Combined sources
Helixi178 – 18710Combined sources
Beta strandi197 – 2015Combined sources
Helixi207 – 2093Combined sources
Helixi210 – 2178Combined sources
Beta strandi224 – 23512Combined sources
Beta strandi238 – 24710Combined sources
Turni251 – 2533Combined sources
Beta strandi257 – 2615Combined sources
Beta strandi291 – 2955Combined sources
Helixi300 – 3078Combined sources
Turni313 – 3164Combined sources
Helixi317 – 3204Combined sources
Turni321 – 3233Combined sources
Beta strandi324 – 3296Combined sources
Turni334 – 3363Combined sources
Helixi337 – 3426Combined sources
Beta strandi350 – 3545Combined sources
Turni358 – 3603Combined sources
Beta strandi365 – 3684Combined sources
Beta strandi372 – 3743Combined sources
Helixi378 – 39013Combined sources
Helixi395 – 3984Combined sources
Helixi399 – 4013Combined sources
Helixi402 – 41413Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KYHX-ray3.00C/D1-459[»]
ProteinModelPortaliQ01159.
SMRiQ01159. Positions 11-415.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01159.

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic GTase family.Curated

Phylogenomic databases

GeneTreeiENSGT00530000063473.
HOGENOMiHOG000162728.
InParanoidiQ01159.
KOiK00987.
OMAiKPPEENT.
OrthoDBiEOG786HCM.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR001339. mRNA_cap_enzyme.
IPR013846. mRNA_cap_enzyme_C.
IPR017075. mRNA_capping_enz_asu.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamiPF03919. mRNA_cap_C. 1 hit.
PF01331. mRNA_cap_enzyme. 1 hit.
[Graphical view]
PIRSFiPIRSF036959. mRNA_cap_alpha. 1 hit.
SUPFAMiSSF50249. SSF50249. 1 hit.

Sequencei

Sequence statusi: Complete.

Q01159-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLAMESRVA PEIPGLIQPG NVTQDLKMMV CKLLNSPKPT KTFPGSQPVS
60 70 80 90 100
FQHSDVEEKL LAHDYYVCEK TDGLRVLMFI VINPVTGEQG CFMIDRENNY
110 120 130 140 150
YLVNGFRFPR LPQKKKEELL ETLQDGTLLD GELVIQTNPM TKLQELRYLM
160 170 180 190 200
FDCLAINGRC LTQSPTSSRL AHLGKEFFKP YFDLRAAYPN RCTTFPFKIS
210 220 230 240 250
MKHMDFSYQL VKVAKSLDKL PHLSDGLIFT PVKAPYTAGG KDSLLLKWKP
260 270 280 290 300
EQENTVDFKL ILDIPMVEDP SLPKDDRNRW YYNYDVKPVF SLYVWQGGAD
310 320 330 340 350
VNSRLKHFDQ PFDRKEFEIL ERTYRKFAEL SVSDEEWQNL KNLEQPLNGR
360 370 380 390 400
IVECAKNQET GAWEMLRFRD DKLNGNHTSV VQKVLESIND SVSLEDLEEI
410 420 430 440 450
VGDIKRCWDE RRANMAGGSG RPLPSQSQNA TLSTSKPVHS QPPSNDKEPK

YVDEDDWSD
Length:459
Mass (Da):52,764
Last modified:February 1, 1995 - v2
Checksum:iF7F5A3E59EEFA15F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451G → S (PubMed:7500935).Curated
Sequence conflicti300 – 3001D → N (PubMed:7500935).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10263 Genomic DNA. Translation: BAA01103.1.
X87252 Genomic DNA. Translation: CAA60705.1.
Z72652 Genomic DNA. Translation: CAA96839.1.
BK006941 Genomic DNA. Translation: DAA07979.1.
PIRiS59731.
RefSeqiNP_011385.3. NM_001180995.3.

Genome annotation databases

EnsemblFungiiYGL130W; YGL130W; YGL130W.
GeneIDi852747.
KEGGisce:YGL130W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10263 Genomic DNA. Translation: BAA01103.1.
X87252 Genomic DNA. Translation: CAA60705.1.
Z72652 Genomic DNA. Translation: CAA96839.1.
BK006941 Genomic DNA. Translation: DAA07979.1.
PIRiS59731.
RefSeqiNP_011385.3. NM_001180995.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KYHX-ray3.00C/D1-459[»]
ProteinModelPortaliQ01159.
SMRiQ01159. Positions 11-415.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33121. 86 interactions.
DIPiDIP-2298N.
IntActiQ01159. 26 interactions.
MINTiMINT-621589.

PTM databases

iPTMnetiQ01159.

Proteomic databases

MaxQBiQ01159.
PeptideAtlasiQ01159.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL130W; YGL130W; YGL130W.
GeneIDi852747.
KEGGisce:YGL130W.

Organism-specific databases

EuPathDBiFungiDB:YGL130W.
SGDiS000003098. CEG1.

Phylogenomic databases

GeneTreeiENSGT00530000063473.
HOGENOMiHOG000162728.
InParanoidiQ01159.
KOiK00987.
OMAiKPPEENT.
OrthoDBiEOG786HCM.

Enzyme and pathway databases

BioCyciMetaCyc:G3O-30626-MONOMER.
YEAST:G3O-30626-MONOMER.
ReactomeiR-SCE-72086. mRNA Capping.
R-SCE-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Miscellaneous databases

EvolutionaryTraceiQ01159.
PROiQ01159.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR001339. mRNA_cap_enzyme.
IPR013846. mRNA_cap_enzyme_C.
IPR017075. mRNA_capping_enz_asu.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamiPF03919. mRNA_cap_C. 1 hit.
PF01331. mRNA_cap_enzyme. 1 hit.
[Graphical view]
PIRSFiPIRSF036959. mRNA_cap_alpha. 1 hit.
SUPFAMiSSF50249. SSF50249. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "mRNA capping enzyme. Isolation and characterization of the gene encoding mRNA guanylytransferase subunit from Saccharomyces cerevisiae."
    Shibagaki Y., Itoh N., Yamada H., Nagata S., Mizumoto K.
    J. Biol. Chem. 267:9521-9528(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DBY939.
  2. Mizumoto K.
    Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 29-30.
  3. "Isolation of temperature-sensitive mutants for mRNA capping enzyme in Saccharomyces cerevisiae."
    Yamagishi M., Mizumoto K., Ishihama A.
    Mol. Gen. Genet. 249:147-154(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Sequence analysis of a 10 kb DNA fragment from yeast chromosome VII reveals a novel member of the DnaJ family."
    Rodriguez-Belmonte E., Rodriguez Torres A.M., Tizon B., Cadahia J.L., Gonzalez-Siso I., Ramil E., Becerra M., Gonzalez-Dominguez M., Cerdan E.
    Yeast 12:145-148(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. "Covalent catalysis in nucleotidyl transfer reactions: essential motifs in Saccharomyces cerevisiae RNA capping enzyme are conserved in Schizosaccharomyces pombe and viral capping enzymes and among polynucleotide ligases."
    Shuman S., Liu Y., Schwer B.
    Proc. Natl. Acad. Sci. U.S.A. 91:12046-12050(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  8. "Active site of the mRNA-capping enzyme guanylyltransferase from Saccharomyces cerevisiae: similarity to the nucleotidyl attachment motif of DNA and RNA ligases."
    Fresco L.D., Buratowski S.
    Proc. Natl. Acad. Sci. U.S.A. 91:6624-6628(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE, MUTAGENESIS OF LYS-59 AND LYS-70.
  9. "Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. I. Purification and subunit structure."
    Itoh N., Mizumoto K., Kaziro Y.
    J. Biol. Chem. 259:13923-13929(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  10. "Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. II. Catalytic properties."
    Itoh N., Mizumoto K., Kaziro Y.
    J. Biol. Chem. 259:13930-13936(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  11. "Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. Large scale purification, subunit functions, and subcellular localization."
    Itoh N., Yamada H., Kaziro Y., Mizumoto K.
    J. Biol. Chem. 262:1989-1995(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMCE1_YEAST
AccessioniPrimary (citable) accession number: Q01159
Secondary accession number(s): D6VU18, Q9URD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1995
Last modified: June 8, 2016
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 279 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.